Evidence map›Paper›PMID 7706415›Full record

ReviewJournal of muscle research and cell motility1994

Role of myosin light chains.

K M Trybus

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Structural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Heavy and light roles: myosin in the morphogenesis of the heart.Cellular and molecular life sciences : CMLS · 2013
    Review
  18. Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

K M TrybusRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham MA 02254-9110.
Brandeis University · US

Funding

SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
NHLBI NIH HHS HL38113
6 · The paper itself

Abstract

All conventional myosin IIs, whether isolated from skeletal, smooth, or invertebrate muscle sources, have two heads attached to an extended 16 nm alpha-helical coiled-coil tail. The head can be divided into a globular motor domain of approximately 770 amino acids that contains the catalytic and actin binding sites, and a neck region of approximately 70 amino acids which binds one essential and one regulatory light chain (ELC and RLC). The neck region with its associated LCs plays both structural and regulatory roles. While the mechanism and extent of regulation by the LCs varies for different myosins, the structural role may be a more fundamental feature of myosin II motors. Our understanding of the neck region has advanced rapidly in recent years primarily because of two types of information: (1) the high resolution structures of the LC binding domain from the thick-filament regulated scallop myosin (Xie et al., 1994) and of the head of unregulated skeletal myosin (Rayment et al., 1993), and (2) the ability to remove and/or mutate portions of both the heavy and light chains for analysis by in vitro motility assays.

Indexed as

Amino Acid SequenceAnimalsFungal ProteinsHumansModels, MolecularMolecular Sequence DataMolluscaMuscle ContractionMyosinsPhosphorylationProtein ConformationProtein Processing, Post-TranslationalFungal ProteinsMyosins

Identifiers

PMID7706415
OpenAlexW2047510044

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.